ID   RIP2_BRYDI              Reviewed;         282 AA.
AC   P98184; Q9S8J0;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Ribosome-inactivating protein bryodin II;
DE            EC=3.2.2.22;
DE   AltName: Full=BD2;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Precursor;
OS   Bryonia dioica (Red bryony) (Bryonia cretica subsp. dioica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Bryonieae; Bryonia.
OX   NCBI_TaxID=3652;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Siegall C.B., Gawlak S.L., Marquardt H.;
RT   "Bryodin 2 a ribosome-inactivating protein isolated from the plant Bryonia
RT   dioica.";
RL   Patent number US5597569, 28-JAN-1997.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-42.
RC   TISSUE=Root;
RX   PubMed=7849072; DOI=10.1021/bc00029a008;
RA   Siegall C.B., Gawlak S.L., Chace D., Wolff E.A., Mixan B., Marquardt H.;
RT   "Characterization of ribosome-inactivating proteins isolated from Bryonia
RT   dioica and their utility as carcinoma-reactive immunoconjugates.";
RL   Bioconj. Chem. 5:423-429(1994).
CC   -!- FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein
CC       synthesis in animal cells. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC         adenosine on the 28S rRNA.; EC=3.2.2.22;
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; I34238; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   AlphaFoldDB; P98184; -.
DR   SMR; P98184; -.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.420.10; -; 1.
DR   Gene3D; 4.10.470.10; -; 1.
DR   InterPro; IPR036041; Ribosome-inact_prot_sf.
DR   InterPro; IPR017989; Ribosome_inactivat_1/2.
DR   InterPro; IPR001574; Ribosome_inactivat_prot.
DR   InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR   InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR   InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR   PANTHER; PTHR33453; PTHR33453; 1.
DR   Pfam; PF00161; RIP; 1.
DR   PRINTS; PR00396; SHIGARICIN.
DR   SUPFAM; SSF56371; SSF56371; 1.
DR   PROSITE; PS00275; SHIGA_RICIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:7849072"
FT   CHAIN           22..282
FT                   /note="Ribosome-inactivating protein bryodin II"
FT                   /id="PRO_0000030756"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   282 AA;  30754 MW;  C52BE2F6A873769C CRC64;
     MRSIGFYSVL ALYVGAHVTE DVDINFSLIG ATGATYKTFI RNLRTKLTVG TPRVYDIPVL
     RNAAAGLARF QLVTLTNYNG ESVTVALDVV NVYVVAYRAG NTAYFLADAS TEANNVLFAG
     INHVRLPYGG NYDGLETAAG RISRENIELG FSEISSAIGN MFRHNPGTSV PRAFIVIIQT
     VSEAARFKYI EQRVSENVGT KFKPDPAFLS LQNAWGSLSE QIQIAQTRGG EFARPVELRT
     VSNTPTFVTN VNSPVVKGIA LLLYFRVNVG TDNVFAMSLS TY